NAC30_ARATH
ID NAC30_ARATH Reviewed; 324 AA.
AC Q9C8W9;
DT 27-MAY-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 25-MAY-2022, entry version 123.
DE RecName: Full=NAC domain-containing protein 30 {ECO:0000303|PubMed:15029955};
DE Short=ANAC030 {ECO:0000303|PubMed:15029955};
DE AltName: Full=Protein VASCULAR RELATED NAC-DOMAIN 7 {ECO:0000303|PubMed:16103214};
GN Name=NAC030 {ECO:0000303|PubMed:15029955};
GN Synonyms=VND7 {ECO:0000303|PubMed:16103214};
GN OrderedLocusNames=At1g71930 {ECO:0000312|Araport:AT1G71930};
GN ORFNames=F17M19.8 {ECO:0000312|EMBL:AAG52219.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702 {ECO:0000312|Proteomes:UP000006548};
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Quinitio C., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF Clones.";
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=15029955; DOI=10.1093/dnares/10.6.239;
RA Ooka H., Satoh K., Doi K., Nagata T., Otomo Y., Murakami K., Matsubara K.,
RA Osato N., Kawai J., Carninci P., Hayashizaki Y., Suzuki K., Kojima K.,
RA Takahara Y., Yamamoto K., Kikuchi S.;
RT "Comprehensive analysis of NAC family genes in Oryza sativa and Arabidopsis
RT thaliana.";
RL DNA Res. 10:239-247(2003).
RN [6]
RP FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP SUBCELLULAR LOCATION, INDUCTION BY BRASSINOSTEROIDS; AUXIN AND CYTOKININ,
RP GENE FAMILY, AND NOMENCLATURE.
RC STRAIN=cv. Columbia;
RX PubMed=16103214; DOI=10.1101/gad.1331305;
RA Kubo M., Udagawa M., Nishikubo N., Horiguchi G., Yamaguchi M., Ito J.,
RA Mimura T., Fukuda H., Demura T.;
RT "Transcription switches for protoxylem and metaxylem vessel formation.";
RL Genes Dev. 19:1855-1860(2005).
RN [7]
RP TISSUE SPECIFICITY.
RX PubMed=16581911; DOI=10.1073/pnas.0510607103;
RA Lee J.-Y., Colinas J., Wang J.Y., Mace D., Ohler U., Benfey P.N.;
RT "Transcriptional and posttranscriptional regulation of transcription factor
RT expression in Arabidopsis roots.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:6055-6060(2006).
RN [8]
RP FUNCTION.
RX PubMed=17890373; DOI=10.1105/tpc.107.053678;
RA Zhong R., Richardson E.A., Ye Z.-H.;
RT "The MYB46 transcription factor is a direct target of SND1 and regulates
RT secondary wall biosynthesis in Arabidopsis.";
RL Plant Cell 19:2776-2792(2007).
RN [9]
RP TISSUE SPECIFICITY.
RX PubMed=17565617; DOI=10.1111/j.1365-313x.2007.03109.x;
RA Ko J.-H., Yang S.H., Park A.H., Lerouxel O., Han K.-H.;
RT "ANAC012, a member of the plant-specific NAC transcription factor family,
RT negatively regulates xylary fiber development in Arabidopsis thaliana.";
RL Plant J. 50:1035-1048(2007).
RN [10]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=18952777; DOI=10.1105/tpc.108.061325;
RA Zhong R., Lee C., Zhou J., McCarthy R.L., Ye Z.H.;
RT "A battery of transcription factors involved in the regulation of secondary
RT cell wall biosynthesis in Arabidopsis.";
RL Plant Cell 20:2763-2782(2008).
RN [11]
RP INDUCTION BY ASL20, AND FUNCTION.
RX PubMed=19088331; DOI=10.1105/tpc.108.061796;
RA Soyano T., Thitamadee S., Machida Y., Chua N.-H.;
RT "ASYMMETRIC LEAVES2-LIKE19/LATERAL ORGAN BOUNDARIES DOMAIN30 and
RT ASL20/LBD18 regulate tracheary element differentiation in Arabidopsis.";
RL Plant Cell 20:3359-3373(2008).
RN [12]
RP FUNCTION, DISRUPTION PHENOTYPE, INTERACTION WITH NAC037/VND1; NAC076/VND2
RP AND NAC105/VND3, HOMODIMER, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP DEVELOPMENTAL STAGE, AND REGULATION BY PROTEASOME DEGRADATION.
RC STRAIN=cv. Columbia;
RX PubMed=18445131; DOI=10.1111/j.1365-313x.2008.03533.x;
RA Yamaguchi M., Kubo M., Fukuda H., Demura T.;
RT "Vascular-related NAC-DOMAIN7 is involved in the differentiation of all
RT types of xylem vessels in Arabidopsis roots and shoots.";
RL Plant J. 55:652-664(2008).
RN [13]
RP FUNCTION.
RC STRAIN=cv. Columbia;
RX PubMed=19122102; DOI=10.1105/tpc.108.063321;
RA Zhou J., Lee C., Zhong R., Ye Z.-H.;
RT "MYB58 and MYB63 are transcriptional activators of the lignin biosynthetic
RT pathway during secondary cell wall formation in Arabidopsis.";
RL Plant Cell 21:248-266(2009).
RN [14]
RP FUNCTION.
RX PubMed=19808805; DOI=10.1093/pcp/pcp139;
RA McCarthy R.L., Zhong R., Ye Z.-H.;
RT "MYB83 is a direct target of SND1 and acts redundantly with MYB46 in the
RT regulation of secondary cell wall biosynthesis in Arabidopsis.";
RL Plant Cell Physiol. 50:1950-1964(2009).
RN [15]
RP FUNCTION.
RX PubMed=20935069; DOI=10.1093/mp/ssq062;
RA Zhong R., Lee C., Ye Z.-H.;
RT "Global analysis of direct targets of secondary wall NAC master switches in
RT Arabidopsis.";
RL Mol. Plant 3:1087-1103(2010).
RN [16]
RP INTERACTION WITH NAC083/VNI2.
RX PubMed=20388856; DOI=10.1105/tpc.108.064048;
RA Yamaguchi M., Ohtani M., Mitsuda N., Kubo M., Ohme-Takagi M., Fukuda H.,
RA Demura T.;
RT "VND-INTERACTING2, a NAC domain transcription factor, negatively regulates
RT xylem vessel formation in Arabidopsis.";
RL Plant Cell 22:1249-1263(2010).
RN [17]
RP FUNCTION.
RX PubMed=20488898; DOI=10.1104/pp.110.154013;
RA Yamaguchi M., Goue N., Igarashi H., Ohtani M., Nakano Y., Mortimer J.C.,
RA Nishikubo N., Kubo M., Katayama Y., Kakegawa K., Dupree P., Demura T.;
RT "VASCULAR-RELATED NAC-DOMAIN6 and VASCULAR-RELATED NAC-DOMAIN7 effectively
RT induce transdifferentiation into xylem vessel elements under control of an
RT induction system.";
RL Plant Physiol. 153:906-914(2010).
RN [18]
RP FUNCTION.
RX PubMed=22037706; DOI=10.1038/nmeth.1750;
RA Gaudinier A., Zhang L., Reece-Hoyes J.S., Taylor-Teeples M., Pu L., Liu Z.,
RA Breton G., Pruneda-Paz J.L., Kim D., Kay S.A., Walhout A.J.M., Ware D.,
RA Brady S.M.;
RT "Enhanced Y1H assays for Arabidopsis.";
RL Nat. Methods 8:1053-1055(2011).
RN [19]
RP FUNCTION, AND REPRESSION BY WEE1.
RC STRAIN=cv. Columbia;
RX PubMed=21498679; DOI=10.1105/tpc.110.082768;
RA Cools T., Iantcheva A., Weimer A.K., Boens S., Takahashi N., Maes S.,
RA Van den Daele H., Van Isterdael G., Schnittger A., De Veylder L.;
RT "The Arabidopsis thaliana checkpoint kinase WEE1 protects against premature
RT vascular differentiation during replication stress.";
RL Plant Cell 23:1435-1448(2011).
RN [20]
RP FUNCTION.
RX PubMed=21284754; DOI=10.1111/j.1365-313x.2011.04514.x;
RA Yamaguchi M., Mitsuda N., Ohtani M., Ohme-Takagi M., Kato K., Demura T.;
RT "VASCULAR-RELATED NAC-DOMAIN7 directly regulates the expression of a broad
RT range of genes for xylem vessel formation.";
RL Plant J. 66:579-590(2011).
RN [21]
RP REVIEW.
RX PubMed=21847026; DOI=10.4161/psb.6.9.16402;
RA McCarthy R.L., Zhong R., Ye Z.-H.;
RT "Secondary wall NAC binding element (SNBE), a key cis-acting element
RT required for target gene activation by secondary wall NAC master
RT switches.";
RL Plant Signal. Behav. 6:1282-1285(2011).
RN [22]
RP FUNCTION, AND INDUCTION BY VERTICILLIUM LONGISPORUM.
RC STRAIN=cv. Columbia;
RX PubMed=23023171; DOI=10.1105/tpc.112.103374;
RA Reusche M., Thole K., Janz D., Truskina J., Rindfleisch S., Drubert C.,
RA Polle A., Lipka V., Teichmann T.;
RT "Verticillium infection triggers VASCULAR-RELATED NAC DOMAIN7-dependent de
RT novo xylem formation and enhances drought tolerance in Arabidopsis.";
RL Plant Cell 24:3823-3837(2012).
RN [23]
RP INDUCTION BY AUXIN.
RX PubMed=22345435; DOI=10.1093/pcp/pcs017;
RA Yoshimoto K., Noutoshi Y., Hayashi K., Shirasu K., Takahashi T., Motose H.;
RT "A chemical biology approach reveals an opposite action between
RT thermospermine and auxin in xylem development in Arabidopsis thaliana.";
RL Plant Cell Physiol. 53:635-645(2012).
CC -!- FUNCTION: Transcription activator that binds to the secondary wall NAC
CC binding element (SNBE), 5'-
CC (T/A)NN(C/T)(T/C/G)TNNNNNNNA(A/C)GN(A/C/T)(A/T)-3', in the promoter of
CC target genes (e.g. genes involved in secondary wall biosynthesis, cell
CC wall modification such as xylan accumulation, and programmed cell
CC death) (PubMed:20935069, PubMed:20488898, PubMed:22037706,
CC PubMed:21284754). Involved in xylem formation in roots and shoots,
CC especially regulating protoxylem vessel differentiation by promoting
CC immature xylem vessel-specific genes expression (PubMed:16103214,
CC PubMed:18445131, PubMed:20488898, PubMed:21498679, PubMed:21284754).
CC Can activate the expression of several genes including XCP1, MYB46,
CC NAC010/SND3, MYB103, MYB58, MYB63, MYB83, KNAT7, ASL19 and ASL20
CC (PubMed:17890373, PubMed:19088331, PubMed:18952777, PubMed:19122102,
CC PubMed:19808805, PubMed:20935069, PubMed:21284754).
CC {ECO:0000269|PubMed:16103214, ECO:0000269|PubMed:17890373,
CC ECO:0000269|PubMed:18445131, ECO:0000269|PubMed:18952777,
CC ECO:0000269|PubMed:19088331, ECO:0000269|PubMed:19122102,
CC ECO:0000269|PubMed:19808805, ECO:0000269|PubMed:20488898,
CC ECO:0000269|PubMed:20935069, ECO:0000269|PubMed:21284754,
CC ECO:0000269|PubMed:21498679, ECO:0000269|PubMed:22037706}.
CC -!- FUNCTION: Required for the soilborne fungal pathogen Verticillium
CC longisporum-induced transdifferentiation of chloroplast-containing
CC bundle sheath cells to functional xylem elements leading to stunted
CC growth, vein clearing, and leaf chloroses, as well as xylem hyperplasia
CC within the vasculature of leaves, hypocotyls, and roots due to
CC reinitiation of cambial activity and transdifferentiation of xylem
CC parenchyma cells. This developmental reprogramming mediates also an
CC increased drought stress tolerance. {ECO:0000269|PubMed:23023171}.
CC -!- SUBUNIT: Forms homodimer and heterodimers with other VND proteins (e.g.
CC NAC037/VND1, NAC076/VND2 and NAC105/VND3) via their N-termini
CC (PubMed:18445131). Interacts with NAC083/VNI2 (PubMed:20388856).
CC {ECO:0000269|PubMed:18445131, ECO:0000269|PubMed:20388856}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00353,
CC ECO:0000269|PubMed:16103214, ECO:0000269|PubMed:18445131}.
CC -!- TISSUE SPECIFICITY: Expressed in developing protoxylems in roots and
CC shoots (PubMed:16103214, PubMed:16581911, PubMed:17565617,
CC PubMed:18952777). Detected in root protoxylem poles and in vessels of
CC protoxylems, outermost metaxylems, inner metaxylems, shoots and
CC hypocotyls. Expressed in roots, hypocotyls, cotyledons and leaves
CC (PubMed:18445131). Accumulates in the xylem but not in interfascicular
CC fibers or pith cells in inflorescence stems. Present in developing
CC vessels of the secondary xylem in roots undergoing secondary growth
CC (PubMed:18952777). {ECO:0000269|PubMed:16103214,
CC ECO:0000269|PubMed:16581911, ECO:0000269|PubMed:17565617,
CC ECO:0000269|PubMed:18445131, ECO:0000269|PubMed:18952777}.
CC -!- DEVELOPMENTAL STAGE: Predominantly expressed in immature xylem vessels,
CC only in some cells just beside xylem vessels. Also present in various
CC vascular cells of older part of the roots, near the location of
CC emergence of the lateral roots. {ECO:0000269|PubMed:16103214,
CC ECO:0000269|PubMed:18445131}.
CC -!- INDUCTION: By brassinosteroids (e.g. brassinolide BL), auxin (e.g. 2,4-
CC dichlorphenoxyacetic acid 2,4-D) and cytokinin (e.g. kinetin), with a
CC synergistic effect (PubMed:16103214, PubMed:22345435). Up-regulated in
CC a feed-back loop by ASL20 (PubMed:19088331). Levels are monitored by
CC proteasome-mediated degradation (PubMed:18445131). Repressed by WEE1
CC upon replication stress to prevent premature tracheary element
CC differentiation (PubMed:21498679). Accumulates during infection by the
CC soilborne fungal pathogen Verticillium longisporum, especially in
CC tissues undergoing de novo xylem formation (PubMed:23023171).
CC {ECO:0000269|PubMed:16103214, ECO:0000269|PubMed:18445131,
CC ECO:0000269|PubMed:19088331, ECO:0000269|PubMed:21498679,
CC ECO:0000269|PubMed:22345435, ECO:0000269|PubMed:23023171}.
CC -!- DOMAIN: The NAC domain includes a DNA binding domain and a dimerization
CC domain. {ECO:0000255|PROSITE-ProRule:PRU00353}.
CC -!- DISRUPTION PHENOTYPE: Defects in protoxylem vessel formation in
CC seedling roots. {ECO:0000269|PubMed:16103214,
CC ECO:0000269|PubMed:18445131}.
CC -!- SIMILARITY: Belongs to the plant vascular related NAC-domain protein
CC family. {ECO:0000305}.
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DR EMBL; AC021665; AAG52219.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE35254.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM61162.1; -; Genomic_DNA.
DR EMBL; BT026447; ABH04554.1; -; mRNA.
DR EMBL; AY085424; AAM62651.1; -; mRNA.
DR PIR; B96742; B96742.
DR RefSeq; NP_001323397.1; NM_001334512.1.
DR RefSeq; NP_177338.1; NM_105851.2.
DR AlphaFoldDB; Q9C8W9; -.
DR SMR; Q9C8W9; -.
DR IntAct; Q9C8W9; 6.
DR STRING; 3702.AT1G71930.1; -.
DR PaxDb; Q9C8W9; -.
DR PRIDE; Q9C8W9; -.
DR ProteomicsDB; 251198; -.
DR EnsemblPlants; AT1G71930.1; AT1G71930.1; AT1G71930.
DR EnsemblPlants; AT1G71930.2; AT1G71930.2; AT1G71930.
DR GeneID; 843524; -.
DR Gramene; AT1G71930.1; AT1G71930.1; AT1G71930.
DR Gramene; AT1G71930.2; AT1G71930.2; AT1G71930.
DR KEGG; ath:AT1G71930; -.
DR Araport; AT1G71930; -.
DR TAIR; locus:2016049; AT1G71930.
DR eggNOG; ENOG502QUJ2; Eukaryota.
DR HOGENOM; CLU_035664_1_2_1; -.
DR InParanoid; Q9C8W9; -.
DR OMA; QTVMDKQ; -.
DR OrthoDB; 908588at2759; -.
DR PhylomeDB; Q9C8W9; -.
DR PRO; PR:Q9C8W9; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9C8W9; baseline and differential.
DR Genevisible; Q9C8W9; AT.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:UniProtKB.
DR GO; GO:0046982; F:protein heterodimerization activity; IDA:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:UniProtKB.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IPI:TAIR.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0071365; P:cellular response to auxin stimulus; IDA:UniProtKB.
DR GO; GO:0050832; P:defense response to fungus; IMP:UniProtKB.
DR GO; GO:0010628; P:positive regulation of gene expression; IDA:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:TAIR.
DR GO; GO:0090059; P:protoxylem development; IMP:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; TAS:TAIR.
DR GO; GO:0009737; P:response to abscisic acid; IEP:TAIR.
DR GO; GO:0009733; P:response to auxin; IEP:UniProtKB.
DR GO; GO:0009741; P:response to brassinosteroid; IEP:TAIR.
DR GO; GO:0009735; P:response to cytokinin; IEP:TAIR.
DR GO; GO:0009620; P:response to fungus; IDA:UniProtKB.
DR GO; GO:0045491; P:xylan metabolic process; IMP:UniProtKB.
DR GO; GO:0010089; P:xylem development; IMP:TAIR.
DR GO; GO:0048759; P:xylem vessel member cell differentiation; IDA:UniProtKB.
DR Gene3D; 2.170.150.80; -; 1.
DR InterPro; IPR003441; NAC-dom.
DR InterPro; IPR036093; NAC_dom_sf.
DR Pfam; PF02365; NAM; 1.
DR SUPFAM; SSF101941; SSF101941; 1.
DR PROSITE; PS51005; NAC; 1.
PE 1: Evidence at protein level;
KW Activator; Cell wall biogenesis/degradation; Developmental protein;
KW DNA-binding; Nucleus; Plant defense; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..324
FT /note="NAC domain-containing protein 30"
FT /id="PRO_0000433120"
FT DOMAIN 9..158
FT /note="NAC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00353"
FT DNA_BIND 109..164
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00353"
FT REGION 232..259
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 232..250
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 324 AA; 37427 MW; C8D3CECD93A59F37 CRC64;
MDNIMQSSMP PGFRFHPTEE ELVGYYLDRK INSMKSALDV IVEIDLYKME PWDIQARCKL
GYEEQNEWYF FSHKDRKYPT GTRTNRATAA GFWKATGRDK AVLSKNSVIG MRKTLVYYKG
RAPNGRKSDW IMHEYRLQNS ELAPVQEEGW VVCRAFRKPI PNQRPLGYEP WQNQLYHVES
SNNYSSSVTM NTSHHIGASS SSHNLNQMLM SNNHYNPNNT SSSMHQYGNI ELPQLDSPSL
SPSLGTNKDQ NESFEQEEEK SFNCVDWRTL DTLLETQVIH PHNPNILMFE TQSYNPAPSF
PSMHQSYNEV EANIHHSLGC FPDS
